ArticleFEBS open bio2022
O-GlcNAcylation regulates lysophosphatidic acid-induced cell migration by regulating ERM family proteins.
Article in FEBS open bio, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
3 citing papers in PubMed, 2 citations in OpenAlex.
- O-glycosylation in Cancer: Emerging Paradigms and Prospects for Precision Oncology.International journal of biological sciences · 2026Review
- O-GlcNAcylation in ovarian tumorigenesis and its therapeutic implications.Translational oncology · 2025Review
- The Emerging Role of LPA as an Oncometabolite.Cells · 2024Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
2 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
O-GlcNAcylation of intracellular proteins (O-GlcNAc) is a post-translational modification that often competes with phosphorylation in diverse cellular signaling pathways. Recent studies on human malignant tumors have demonstrated that O-GlcNAc is implicated in cellular features relevant to metastasis. Here, we report that lysophosphatidic acid (LPA)-induced ovarian cancer cell (OVCAR-3) migration is regulated by O-GlcNAc. We found that O-GlcNAc modification of ERM family proteins, a membrane-cytoskeletal crosslinker, was inversely correlated with its phosphorylation status. Moreover, the LPA-induced formation of membrane protrusion structures, as well as the migration of OVCAR-3 cells, was reduced by the accumulation of O-GlcNAc. Collectively, these findings suggest that O-GlcNAc is an essential signaling element controlling ERM family proteins involved in OVCAR-3 cell migration.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.